JPH07507453A - トキソプラズマのｇｐ２８．５蛋白をエンコードする遺伝子のクローン化とその蛋白のペプチド断片とそれらの応用 - Google Patents

トキソプラズマのｇｐ２８．５蛋白をエンコードする遺伝子のクローン化とその蛋白のペプチド断片とそれらの応用

Info

Publication number: JPH07507453A
Authority: JP; Japan
Prior art keywords: amino acids; sequence; sequence seq; antigen; protein
Prior art date: 1992-06-15
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.): Pending

Application number

JP6501195A

Other languages

English (en)

Japanese (ja)

Inventor

セスブロン，マリー−フランス

メルシエール，コリーヌ

カプロン，アンドレ

タルタール，アンドレ

マーエス，ピエレット

Original Assignee

インスティティ　パスツール

インスティティ　パスツール　ド　リール

インスティティ　ナショナール　ド　ラ　サント　エ　ド　ラ　ルシェルシェ　メディカール（アンスルム）

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1992-06-15

Filing date

1993-06-15

Publication date

1995-08-24

1993-06-15 Application filed by インスティティ　パスツール, インスティティ　パスツール　ド　リール, インスティティ　ナショナール　ド　ラ　サント　エ　ド　ラ　ルシェルシェ　メディカール（アンスルム） filed Critical インスティティ　パスツール

1995-08-24 Publication of JPH07507453A publication Critical patent/JPH07507453A/ja

Status Pending legal-status Critical Current

Links

101000871078 Toxoplasma gondii Dense granule protein 2 Proteins 0.000 title claims description 63
108010033276 Peptide Fragments Proteins 0.000 title claims description 11
102000007079 Peptide Fragments Human genes 0.000 title claims description 11
108090000623 proteins and genes Proteins 0.000 title description 25
102000004169 proteins and genes Human genes 0.000 title description 12
238000010367 cloning Methods 0.000 title description 6
108090000765 processed proteins & peptides Proteins 0.000 claims description 56
150000001413 amino acids Chemical class 0.000 claims description 54
239000000427 antigen Substances 0.000 claims description 51
108091007433 antigens Proteins 0.000 claims description 51
102000036639 antigens Human genes 0.000 claims description 51
102000004196 processed proteins & peptides Human genes 0.000 claims description 32
102000007056 Recombinant Fusion Proteins Human genes 0.000 claims description 25
108010008281 Recombinant Fusion Proteins Proteins 0.000 claims description 25
125000001433 C-terminal amino-acid group Chemical group 0.000 claims description 19
229920001184 polypeptide Polymers 0.000 claims description 19
150000007523 nucleic acids Chemical group 0.000 claims description 16
238000004519 manufacturing process Methods 0.000 claims description 11
GOJUJUVQIVIZAV-UHFFFAOYSA-N 2-amino-4,6-dichloropyrimidine-5-carbaldehyde Chemical group NC1=NC(Cl)=C(C=O)C(Cl)=N1 GOJUJUVQIVIZAV-UHFFFAOYSA-N 0.000 claims description 9
239000000203 mixture Substances 0.000 claims description 9
239000013598 vector Substances 0.000 claims description 8
241000223996 Toxoplasma Species 0.000 claims description 7
210000004027 cell Anatomy 0.000 claims description 5
241001465754 Metazoa Species 0.000 claims description 4
230000000890 antigenic effect Effects 0.000 claims description 4
229960005486 vaccine Drugs 0.000 claims description 3
230000001938 anti-toxoplasmal effect Effects 0.000 claims description 2
238000012258 culturing Methods 0.000 claims description 2
210000003527 eukaryotic cell Anatomy 0.000 claims description 2
210000001236 prokaryotic cell Anatomy 0.000 claims description 2
239000002253 acid Substances 0.000 claims 1
150000007513 acids Chemical class 0.000 claims 1
235000001014 amino acid Nutrition 0.000 description 49
210000002966 serum Anatomy 0.000 description 26
239000012634 fragment Substances 0.000 description 16
239000002299 complementary DNA Substances 0.000 description 12
235000018102 proteins Nutrition 0.000 description 11
230000005764 inhibitory process Effects 0.000 description 10
241000699670 Mus sp. Species 0.000 description 9
241000223997 Toxoplasma gondii Species 0.000 description 9
210000004899 c-terminal region Anatomy 0.000 description 9
102000037865 fusion proteins Human genes 0.000 description 8
108020001507 fusion proteins Proteins 0.000 description 8
208000015181 infectious disease Diseases 0.000 description 8
238000000034 method Methods 0.000 description 8
241000588724 Escherichia coli Species 0.000 description 7
238000002835 absorbance Methods 0.000 description 7
230000001154 acute effect Effects 0.000 description 7
238000002965 ELISA Methods 0.000 description 6
241000699666 Mus <mouse, genus> Species 0.000 description 6
230000001684 chronic effect Effects 0.000 description 6
108091032973 (ribonucleotides)n+m Proteins 0.000 description 5
108020004414 DNA Proteins 0.000 description 5
238000012546 transfer Methods 0.000 description 5
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
125000003275 alpha amino acid group Chemical group 0.000 description 4
102000005936 beta-Galactosidase Human genes 0.000 description 4
108010005774 beta-Galactosidase Proteins 0.000 description 4
239000000872 buffer Substances 0.000 description 4
238000010276 construction Methods 0.000 description 4
238000002474 experimental method Methods 0.000 description 4
238000004128 high performance liquid chromatography Methods 0.000 description 4
239000012528 membrane Substances 0.000 description 4
244000045947 parasite Species 0.000 description 4
230000036961 partial effect Effects 0.000 description 4
239000013612 plasmid Substances 0.000 description 4
238000012163 sequencing technique Methods 0.000 description 4
239000002904 solvent Substances 0.000 description 4
238000012360 testing method Methods 0.000 description 4
WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 3
102000018651 Epithelial Cell Adhesion Molecule Human genes 0.000 description 3
108010066687 Epithelial Cell Adhesion Molecule Proteins 0.000 description 3
241000282412 Homo Species 0.000 description 3
201000005485 Toxoplasmosis Diseases 0.000 description 3
239000002671 adjuvant Substances 0.000 description 3
230000003321 amplification Effects 0.000 description 3
230000015572 biosynthetic process Effects 0.000 description 3
238000010790 dilution Methods 0.000 description 3
239000012895 dilution Substances 0.000 description 3
238000002372 labelling Methods 0.000 description 3
238000003199 nucleic acid amplification method Methods 0.000 description 3
108020004707 nucleic acids Proteins 0.000 description 3
102000039446 nucleic acids Human genes 0.000 description 3
239000012264 purified product Substances 0.000 description 3
230000009257 reactivity Effects 0.000 description 3
239000000523 sample Substances 0.000 description 3
238000013518 transcription Methods 0.000 description 3
230000035897 transcription Effects 0.000 description 3
YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 2
241000894006 Bacteria Species 0.000 description 2
101800001415 Bri23 peptide Proteins 0.000 description 2
101800000655 C-terminal peptide Proteins 0.000 description 2
102400000107 C-terminal peptide Human genes 0.000 description 2
108091026890 Coding region Proteins 0.000 description 2
102000053602 DNA Human genes 0.000 description 2
108091028043 Nucleic acid sequence Proteins 0.000 description 2
102000003992 Peroxidases Human genes 0.000 description 2
208000037581 Persistent Infection Diseases 0.000 description 2
101000702488 Rattus norvegicus High affinity cationic amino acid transporter 1 Proteins 0.000 description 2
229960002685 biotin Drugs 0.000 description 2
239000011616 biotin Substances 0.000 description 2
210000000061 bradyzoite Anatomy 0.000 description 2
238000005119 centrifugation Methods 0.000 description 2
238000012512 characterization method Methods 0.000 description 2
238000006243 chemical reaction Methods 0.000 description 2
238000004587 chromatography analysis Methods 0.000 description 2
238000003776 cleavage reaction Methods 0.000 description 2
230000002860 competitive effect Effects 0.000 description 2
238000001514 detection method Methods 0.000 description 2
238000010586 diagram Methods 0.000 description 2
230000029087 digestion Effects 0.000 description 2
230000000694 effects Effects 0.000 description 2
125000000524 functional group Chemical group 0.000 description 2
230000002068 genetic effect Effects 0.000 description 2
PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 2
230000036039 immunity Effects 0.000 description 2
239000002245 particle Substances 0.000 description 2
239000008188 pellet Substances 0.000 description 2
108040007629 peroxidase activity proteins Proteins 0.000 description 2
YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 2
239000011148 porous material Substances 0.000 description 2
239000000047 product Substances 0.000 description 2
230000001681 protective effect Effects 0.000 description 2
230000007017 scission Effects 0.000 description 2
238000012216 screening Methods 0.000 description 2
SQGYOTSLMSWVJD-UHFFFAOYSA-N silver(1+) nitrate Chemical compound [Ag+].[O-]N(=O)=O SQGYOTSLMSWVJD-UHFFFAOYSA-N 0.000 description 2
239000011780 sodium chloride Substances 0.000 description 2
239000000243 solution Substances 0.000 description 2
239000006228 supernatant Substances 0.000 description 2
238000003786 synthesis reaction Methods 0.000 description 2
ZFXYFBGIUFBOJW-UHFFFAOYSA-N theophylline Chemical compound O=C1N(C)C(=O)N(C)C2=C1NC=N2 ZFXYFBGIUFBOJW-UHFFFAOYSA-N 0.000 description 2
230000005026 transcription initiation Effects 0.000 description 2
238000013519 translation Methods 0.000 description 2
XXMFJKNOJSDQBM-UHFFFAOYSA-N 2,2,2-trifluoroacetic acid;hydrate Chemical compound [OH3+].[O-]C(=O)C(F)(F)F XXMFJKNOJSDQBM-UHFFFAOYSA-N 0.000 description 1
NHBKXEKEPDILRR-UHFFFAOYSA-N 2,3-bis(butanoylsulfanyl)propyl butanoate Chemical compound CCCC(=O)OCC(SC(=O)CCC)CSC(=O)CCC NHBKXEKEPDILRR-UHFFFAOYSA-N 0.000 description 1
QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
101710127328 28 kDa antigen Proteins 0.000 description 1
LVSPDZAGCBEQAV-UHFFFAOYSA-N 4-chloronaphthalen-1-ol Chemical compound C1=CC=C2C(O)=CC=C(Cl)C2=C1 LVSPDZAGCBEQAV-UHFFFAOYSA-N 0.000 description 1
101710122462 65 kDa protein Proteins 0.000 description 1
208000030507 AIDS Diseases 0.000 description 1
HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 1
229920000936 Agarose Polymers 0.000 description 1
108010039627 Aprotinin Proteins 0.000 description 1
108091028026 C-DNA Proteins 0.000 description 1
UNPLRYRWJLTVAE-UHFFFAOYSA-N Cloperastine hydrochloride Chemical compound Cl.C1=CC(Cl)=CC=C1C(C=1C=CC=CC=1)OCCN1CCCCC1 UNPLRYRWJLTVAE-UHFFFAOYSA-N 0.000 description 1
108020004705 Codon Proteins 0.000 description 1
208000003322 Coinfection Diseases 0.000 description 1
230000006820 DNA synthesis Effects 0.000 description 1
108700024394 Exon Proteins 0.000 description 1
-1 FMI6 Proteins 0.000 description 1
229920001917 Ficoll Polymers 0.000 description 1
241001669573 Galeorhinus galeus Species 0.000 description 1
102000003886 Glycoproteins Human genes 0.000 description 1
108090000288 Glycoproteins Proteins 0.000 description 1
102100029054 Homeobox protein notochord Human genes 0.000 description 1
101000634521 Homo sapiens Homeobox protein notochord Proteins 0.000 description 1
102100034343 Integrase Human genes 0.000 description 1
108091092195 Intron Proteins 0.000 description 1
QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
WHXSMMKQMYFTQS-UHFFFAOYSA-N Lithium Chemical compound [Li] WHXSMMKQMYFTQS-UHFFFAOYSA-N 0.000 description 1
206010027476 Metastases Diseases 0.000 description 1
102000016943 Muramidase Human genes 0.000 description 1
108010014251 Muramidase Proteins 0.000 description 1
108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
101150008132 NDE1 gene Proteins 0.000 description 1
239000000020 Nitrocellulose Substances 0.000 description 1
108091034117 Oligonucleotide Proteins 0.000 description 1
102000004316 Oxidoreductases Human genes 0.000 description 1
108090000854 Oxidoreductases Proteins 0.000 description 1
108010029485 Protein Isoforms Proteins 0.000 description 1
102000001708 Protein Isoforms Human genes 0.000 description 1
108010076504 Protein Sorting Signals Proteins 0.000 description 1
101710089165 Protein white Proteins 0.000 description 1
206010037075 Protozoal infections Diseases 0.000 description 1
108010092799 RNA-directed DNA polymerase Proteins 0.000 description 1
108091006629 SLC13A2 Proteins 0.000 description 1
240000004808 Saccharomyces cerevisiae Species 0.000 description 1
241000270295 Serpentes Species 0.000 description 1
108020004682 Single-Stranded DNA Proteins 0.000 description 1
238000002105 Southern blotting Methods 0.000 description 1
108020005038 Terminator Codon Proteins 0.000 description 1
239000007983 Tris buffer Substances 0.000 description 1
229920004890 Triton X-100 Polymers 0.000 description 1
239000013504 Triton X-100 Substances 0.000 description 1
241000677635 Tuxedo Species 0.000 description 1
XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 1
241000700605 Viruses Species 0.000 description 1
206010000210 abortion Diseases 0.000 description 1
231100000176 abortion Toxicity 0.000 description 1
238000001042 affinity chromatography Methods 0.000 description 1
235000004279 alanine Nutrition 0.000 description 1
230000003110 anti-inflammatory effect Effects 0.000 description 1
238000013459 approach Methods 0.000 description 1
229960004405 aprotinin Drugs 0.000 description 1
238000003491 array Methods 0.000 description 1
210000003567 ascitic fluid Anatomy 0.000 description 1
101150030721 ata gene Proteins 0.000 description 1
210000003719 b-lymphocyte Anatomy 0.000 description 1
235000020958 biotin Nutrition 0.000 description 1
210000004369 blood Anatomy 0.000 description 1
239000008280 blood Substances 0.000 description 1
210000000601 blood cell Anatomy 0.000 description 1
244000309466 calf Species 0.000 description 1
239000004202 carbamide Substances 0.000 description 1
150000001720 carbohydrates Chemical class 0.000 description 1
125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
229920002678 cellulose Polymers 0.000 description 1
239000001913 cellulose Substances 0.000 description 1
239000003153 chemical reaction reagent Substances 0.000 description 1
238000012875 competitive assay Methods 0.000 description 1
239000000356 contaminant Substances 0.000 description 1
238000012937 correction Methods 0.000 description 1
230000034994 death Effects 0.000 description 1
231100000517 death Toxicity 0.000 description 1
230000007423 decrease Effects 0.000 description 1
230000007123 defense Effects 0.000 description 1
230000007850 degeneration Effects 0.000 description 1
238000011161 development Methods 0.000 description 1
239000000539 dimer Substances 0.000 description 1
238000010828 elution Methods 0.000 description 1
238000011156 evaluation Methods 0.000 description 1
239000013604 expression vector Substances 0.000 description 1
238000000605 extraction Methods 0.000 description 1
230000004927 fusion Effects 0.000 description 1
125000000404 glutamine group Chemical group N[C@@H](CCC(N)=O)C(=O)* 0.000 description 1
229960003180 glutathione Drugs 0.000 description 1
102000035122 glycosylated proteins Human genes 0.000 description 1
108091005608 glycosylated proteins Proteins 0.000 description 1
229910052737 gold Inorganic materials 0.000 description 1
239000010931 gold Substances 0.000 description 1
239000008187 granular material Substances 0.000 description 1
230000001900 immune effect Effects 0.000 description 1
230000003053 immunization Effects 0.000 description 1
238000002649 immunization Methods 0.000 description 1
230000002163 immunogen Effects 0.000 description 1
230000016784 immunoglobulin production Effects 0.000 description 1
238000011534 incubation Methods 0.000 description 1
230000002401 inhibitory effect Effects 0.000 description 1
ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 description 1
239000003999 initiator Substances 0.000 description 1
230000009545 invasion Effects 0.000 description 1
238000010829 isocratic elution Methods 0.000 description 1
BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 1
229910052744 lithium Inorganic materials 0.000 description 1
244000144972 livestock Species 0.000 description 1
230000004807 localization Effects 0.000 description 1
230000005923 long-lasting effect Effects 0.000 description 1
239000006166 lysate Substances 0.000 description 1
230000001320 lysogenic effect Effects 0.000 description 1
229960000274 lysozyme Drugs 0.000 description 1
235000010335 lysozyme Nutrition 0.000 description 1
239000004325 lysozyme Substances 0.000 description 1
230000036244 malformation Effects 0.000 description 1
239000011159 matrix material Substances 0.000 description 1
108020004999 messenger RNA Proteins 0.000 description 1
230000009401 metastasis Effects 0.000 description 1
244000005700 microbiome Species 0.000 description 1
238000010369 molecular cloning Methods 0.000 description 1
239000000178 monomer Substances 0.000 description 1
229920001220 nitrocellulos Polymers 0.000 description 1
230000001473 noxious effect Effects 0.000 description 1
239000004417 polycarbonate Substances 0.000 description 1
229920000515 polycarbonate Polymers 0.000 description 1
229920000642 polymer Polymers 0.000 description 1
230000017854 proteolysis Effects 0.000 description 1
230000002829 reductive effect Effects 0.000 description 1
238000011160 research Methods 0.000 description 1
230000000717 retained effect Effects 0.000 description 1
238000004007 reversed phase HPLC Methods 0.000 description 1
230000028327 secretion Effects 0.000 description 1
229910001961 silver nitrate Inorganic materials 0.000 description 1
238000001179 sorption measurement Methods 0.000 description 1
238000010186 staining Methods 0.000 description 1
238000006467 substitution reaction Methods 0.000 description 1
239000000758 substrate Substances 0.000 description 1
239000000725 suspension Substances 0.000 description 1
210000000059 tachyzoite Anatomy 0.000 description 1
238000001890 transfection Methods 0.000 description 1
230000014621 translational initiation Effects 0.000 description 1
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
241000701447 unidentified baculovirus Species 0.000 description 1
238000011144 upstream manufacturing Methods 0.000 description 1
210000003934 vacuole Anatomy 0.000 description 1
238000012800 visualization Methods 0.000 description 1
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/44—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from protozoa
- C07K14/45—Toxoplasma
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P33/00—Antiparasitic agents
- A61P33/02—Antiprotozoals, e.g. for leishmaniasis, trichomoniasis, toxoplasmosis
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/02—Fusion polypeptide containing a localisation/targetting motif containing a signal sequence
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/20—Fusion polypeptide containing a tag with affinity for a non-protein ligand
- C07K2319/23—Fusion polypeptide containing a tag with affinity for a non-protein ligand containing a GST-tag
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/40—Fusion polypeptide containing a tag for immunodetection, or an epitope for immunisation
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/61—Fusion polypeptide containing an enzyme fusion for detection (lacZ, luciferase)

Landscapes

Health & Medical Sciences (AREA)
Chemical & Material Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Organic Chemistry (AREA)
General Health & Medical Sciences (AREA)
Medicinal Chemistry (AREA)
Veterinary Medicine (AREA)
Public Health (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
Genetics & Genomics (AREA)
Biochemistry (AREA)
Molecular Biology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Gastroenterology & Hepatology (AREA)
Toxicology (AREA)
Zoology (AREA)
Chemical Kinetics & Catalysis (AREA)
General Chemical & Material Sciences (AREA)
Biophysics (AREA)
Pharmacology & Pharmacy (AREA)
Animal Behavior & Ethology (AREA)
Tropical Medicine & Parasitology (AREA)
Communicable Diseases (AREA)
Oncology (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Peptides Or Proteins (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)

JP6501195A 1992-06-15 1993-06-15 トキソプラズマのｇｐ２８．５蛋白をエンコードする遺伝子のクローン化とその蛋白のペプチド断片とそれらの応用 Pending JPH07507453A (ja)

Applications Claiming Priority (3)

Application Number	Priority Date	Filing Date	Title
FR92/07206		1992-06-15
FR9207206A FR2692282B1 (fr)	1992-06-15	1992-06-15	Clonage du gene codant pour la proteine gp28.5 de t. gondii; fragments peptidiques issus de ladite proteine et leurs applications.
PCT/FR1993/000575 WO1993025689A1 (fr)	1992-06-15	1993-06-15	Clonage du gene codant pour la proteine gp28.5 de t. gondii; fragments peptidiques issus de ladite proteine et leurs applications

Publications (1)

Publication Number	Publication Date
JPH07507453A true JPH07507453A (ja)	1995-08-24

Family

ID=9430735

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
JP6501195A Pending JPH07507453A (ja)	1992-06-15	1993-06-15	トキソプラズマのｇｐ２８．５蛋白をエンコードする遺伝子のクローン化とその蛋白のペプチド断片とそれらの応用

Country Status (8)

Country	Link
US (2)	US5824788A (de)
EP (1)	EP0648270B1 (de)
JP (1)	JPH07507453A (de)
AT (1)	ATE314474T1 (de)
CA (1)	CA2137280C (de)
DE (1)	DE69333952D1 (de)
FR (1)	FR2692282B1 (de)
WO (1)	WO1993025689A1 (de)

Families Citing this family (12)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US5665542A (en) *	1989-11-03	1997-09-09	Research Institute Of Palo Alto Medical Foundation	Toxoplasma gondii P28 gene and methods for its use
FR2692282B1 (fr) *	1992-06-15	1995-07-13	Pasteur Institut	Clonage du gene codant pour la proteine gp28.5 de t. gondii; fragments peptidiques issus de ladite proteine et leurs applications.
ZA958366B (en) *	1994-10-06	1996-04-24	Akzo Nobel Nv	New toxoplasma gondii antigens
US6448039B1 (en) *	1995-06-16	2002-09-10	The Board Of Trustees Of The Leland Stanford Junior University	Enhancer sequences for late T cell expressed genes
EP0953641A3 (de) *	1998-03-26	2002-03-13	Pfizer Products Inc.	Für Neospora Proteine kodierende polynukleotid Moleküle
US6902926B1 (en) *	2000-11-09	2005-06-07	University Of Vermont And State Agricultural College	Toxoplasma gondii apical membrane antigen-1
BR0200690A (pt) *	2002-03-04	2004-03-23	Embrapa Pesquisa Agropecuaria	Método para detecção de proteinas de origem em misturas complexas
BR0308620A (pt) *	2002-03-21	2005-02-15	Kenton S R L	Fragmentos de antìgenos para a diagnose de toxoplasma gondii
EP1507004A1 (de) *	2003-08-14	2005-02-16	DKFZ Deutsches Krebsforschungszentrum	Verfahren zur Inhibierung der Vermehrung unerwünschter Zellpopulationen
DK1856159T3 (da) *	2005-03-08	2010-07-05	Sigma Tau Ind Farmaceuti	Kimære, rekombinante antigener af Toxoplasma gondii
EP2654782A4 (de) *	2010-12-23	2015-03-25	Immport Therapeutics Inc	Verfahren und zusammensetzungen aus proteinantigenen zur diagnose und behandlung von toxoplasma-gondii-infektionen und toxoplasmose
FR2996918B1 (fr)	2012-10-16	2015-07-03	Univ Grenoble 1	Antigenes gra recombinants et leur application pour le diagnostic precoce de la toxoplasmose

Family Cites Families (4)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
DE3940598A1 (de) *	1989-12-08	1991-06-13	Behringwerke Ag	Toxoplasma gondii-antigene, ihre herstellung und ihre verwendung
EP0373192B1 (de) *	1988-03-09	1996-06-12	The Board Of Trustees Of The Leland Stanford Junior University	Diagnostische gene zum nachweis von toxoplasmose
US5665542A (en) *	1989-11-03	1997-09-09	Research Institute Of Palo Alto Medical Foundation	Toxoplasma gondii P28 gene and methods for its use
FR2692282B1 (fr) *	1992-06-15	1995-07-13	Pasteur Institut	Clonage du gene codant pour la proteine gp28.5 de t. gondii; fragments peptidiques issus de ladite proteine et leurs applications.

1992
- 1992-06-15 FR FR9207206A patent/FR2692282B1/fr not_active Expired - Fee Related
1993
- 1993-06-15 AT AT93913130T patent/ATE314474T1/de not_active IP Right Cessation
- 1993-06-15 DE DE69333952T patent/DE69333952D1/de not_active Expired - Lifetime
- 1993-06-15 JP JP6501195A patent/JPH07507453A/ja active Pending
- 1993-06-15 EP EP93913130A patent/EP0648270B1/de not_active Expired - Lifetime
- 1993-06-15 WO PCT/FR1993/000575 patent/WO1993025689A1/fr not_active Ceased
- 1993-06-15 CA CA002137280A patent/CA2137280C/fr not_active Expired - Fee Related
- 1993-06-15 US US08/338,543 patent/US5824788A/en not_active Expired - Fee Related
1998
- 1998-06-05 US US09/092,179 patent/US6392014B1/en not_active Expired - Fee Related

Also Published As

Publication number	Publication date
US5824788A (en)	1998-10-20
ATE314474T1 (de)	2006-01-15
WO1993025689A1 (fr)	1993-12-23
FR2692282B1 (fr)	1995-07-13
CA2137280C (fr)	2005-12-27
US6392014B1 (en)	2002-05-21
CA2137280A1 (fr)	1993-12-23
DE69333952D1 (de)	2006-02-02
FR2692282A1 (fr)	1993-12-17
EP0648270B1 (de)	2005-12-28
EP0648270A1 (de)	1995-04-19

Legal Events

Date

Code

Title

Description

2004-01-20

A02

Decision of refusal

Free format text: JAPANESE INTERMEDIATE CODE: A02

Effective date: 20040120

Publication	Publication Date	Title
Lecordier et al.	1995	Characterization of a dense granule antigen of Toxoplasma gondii (GRA6) associated to the network of the parasitophorous vacuole
Bishop et al.	2002	A cement protein of the tick Rhipicephalusappendiculatus, located in the secretory e cell granules of the type III salivary gland acini, induces strong antibody responses in cattle
Mercier et al.	1993	Molecular characterization of a dense granule antigen (Gra 2) associated with the network of the parasitophorous vacuole in Toxoplasma gondii
Banerjee et al.	1996	Molecular cloning and expression of a recombinant Aspergillus fumigatus protein Asp f II with significant immunoglobulin E reactivity in allergic bronchopulmonary aspergillosis
US5824788A (en)	1998-10-20	Cloning of gene encoding the GP28.5 protein of toxoplasma gondii; peptide fragments of said protein and their applications
CN1606565B (zh)	2011-06-29	编码重组的来源于巨型艾美球虫配子母细胞的56和82kDa抗原的核酸和它们的应用
JPH06508994A (ja)	1994-10-13	日本杉花粉からのアレルゲン性蛋白質及びペプチド
Cully et al.	1986	Identification of proteins encoded by variant surface glycoprotein expression site-associated genes in Trypanosoma brucei
MC2227A1 (fr)	1993-02-02	Procede pour preparer une proteine ayant un ou plusieurs determinants immunoreactifs et/ou antigeniques de l'antigene de surface des merozoites d'eimeria,adn codant pour cette proteine,procede de preparation d'un vecteur recombinant comprenant cet adn,procede de preparation d'un microorganisme transforme contenant ce vecteur recombinant et procede pour preparer un vaccin protegeant les volailles contre la coccidiose
JP2812759B2 (ja)	1998-10-22	ヒトマラリアワクチン抗原をコードする遺伝子
US20050095256A1 (en)	2005-05-05	Recombinant process for preparing a complete malaria antigen gp190/MSP1
JP5055522B2 (ja)	2012-10-24	多包条虫由来の新規蛋白質
Atkinson et al.	2001	Isolation of Neospora caninum genes detected during a chronic murine infection
CN101434954A (zh)	2009-05-20	中华蜜蜂王浆主蛋白AccMRJP7基因及其编码蛋白
Nockemann et al.	1998	Expression, characterization and serological reactivity of a 41 kDa excreted–secreted antigen (ESA) from Toxoplasma gondii
US5578714A (en)	1996-11-26	DNA encoding Duffy 9pd protein
US5525508A (en)	1996-06-11	Haemonchus contortus vaccine
EP0780472A2 (de)	1997-06-25	Stress Proteine
EP0215059A1 (de)	1987-03-25	C-dna, kodierend für plasmodium-falciparum-glykophorinbindungsproteine mit einem gewicht von 130000 dalton bzw 155000 dalton
HU211581A9 (en)	1995-12-28	Plasmodium falciparum merozoite antigen-peptide
Hummel et al.	1992	Tetrahymena gene encodes a protein that is homologous with the liver-specific F-antigen and associated with membranes of the Golgi apparatus and transport vesicles
Teuber et al.	1991	The identification and cloning of the murine genes encoding the liver specific F alloantigens
WO2000017351A1 (fr)	2000-03-30	Nouvelle sequence codant pour le facteur de croissance derive de l'hepatome humain et polypeptide code par cette sequence d'adn, et procede de production de ceux-ci
FR2702491A1 (fr)	1994-09-16	Clonage de gènes codant pour des antigènes d'excrétion-sécrétion P21 et P32 de toxoplasme, préparations de tels antigènes, fragments de ceux-ci et leurs applications.
AU697868C (en)	2000-06-01	The cloning of Duffy blood group antigen